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Protein

60S ribosomal protein L23

Gene

RpL23

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • myosin binding Source: FlyBase
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • neurogenesis Source: FlyBase
  • translation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L23
Alternative name(s):
L17A
Gene namesi
Name:RpL23
Synonyms:RpL17A
ORF Names:CG3661
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010078. RpL23.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14014060S ribosomal protein L23PRO_0000128623Add
BLAST

Proteomic databases

PaxDbiP48159.
PRIDEiP48159.

Expressioni

Gene expression databases

BgeeiP48159.
ExpressionAtlasiP48159. differential.
GenevisibleiP48159. DM.

Interactioni

GO - Molecular functioni

  • myosin binding Source: FlyBase

Protein-protein interaction databases

BioGridi63240. 18 interactions.
DIPiDIP-21429N.
IntActiP48159. 20 interactions.
MINTiMINT-943050.
STRINGi7227.FBpp0071808.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CV1-140[»]
ProteinModelPortaliP48159.
SMRiP48159. Positions 11-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
InParanoidiP48159.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP48159.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRGRGGTA GGKFRISLGL PVGAVMNCAD NTGAKNLYVI AVHGIRGRLN
60 70 80 90 100
RLPAAGVGDM FVATVKKGKP ELRKKVMPAV VIRQRKPFRR RDGVFIYFED
110 120 130 140
NAGVIVNNKG EMKGSAITGP VAKECADLWP RIASNASSIA
Length:140
Mass (Da):14,937
Last modified:December 7, 2004 - v2
Checksum:iFC093BAC360924FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 826MPAVVI → SVVPSA in AAA28867 (PubMed:1511900).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85295 Genomic DNA. Translation: AAA28867.1.
AE013599 Genomic DNA. Translation: AAF46914.1.
BT053700 mRNA. Translation: ACK77617.1.
PIRiJC1253.
RefSeqiNP_523813.1. NM_079089.4.
UniGeneiDm.6664.

Genome annotation databases

EnsemblMetazoaiFBtr0071897; FBpp0071808; FBgn0010078.
GeneIDi37628.
KEGGidme:Dmel_CG3661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85295 Genomic DNA. Translation: AAA28867.1.
AE013599 Genomic DNA. Translation: AAF46914.1.
BT053700 mRNA. Translation: ACK77617.1.
PIRiJC1253.
RefSeqiNP_523813.1. NM_079089.4.
UniGeneiDm.6664.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CV1-140[»]
ProteinModelPortaliP48159.
SMRiP48159. Positions 11-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63240. 18 interactions.
DIPiDIP-21429N.
IntActiP48159. 20 interactions.
MINTiMINT-943050.
STRINGi7227.FBpp0071808.

Proteomic databases

PaxDbiP48159.
PRIDEiP48159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071897; FBpp0071808; FBgn0010078.
GeneIDi37628.
KEGGidme:Dmel_CG3661.

Organism-specific databases

CTDi9349.
FlyBaseiFBgn0010078. RpL23.

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
InParanoidiP48159.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP48159.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpL23. fly.
GenomeRNAii37628.
PROiP48159.

Gene expression databases

BgeeiP48159.
ExpressionAtlasiP48159. differential.
GenevisibleiP48159. DM.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila melanogaster ribosomal protein L17A-encoding gene."
    Noselli S., Vincent A.
    Gene 118:273-278(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Ovary.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL23_DROME
AccessioniPrimary (citable) accession number: P48159
Secondary accession number(s): B7FNL0, Q9W1Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.